Lysosomal enzyme activity in rat and beef skeletal muscle

Stagni, N.; Bernard, B. de

doi:10.1016/0304-4165(68)90167-0

Cited by 58 publications

(20 citation statements)

References 22 publications

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“…Acid hydrolases, such as cathepsin and a-glucosidase may be associated with lysosomes in muscle [7,27]. It is of interest, therefore, that whilst acid cathepsin has a higher activity in the EDL than in the soleus (in agreement with the data of Hajek, Gutmann and Syrovy [8] obtained with muscle extracts) the reverse is true for a-glucosid ase.…”

Section: Determination Of Enzyme Activitiessupporting

confidence: 79%

Quantitative Enzyme Studies in Extensor Digitorum Longus and Soleus Muscles of Rats

Goldspink¹,

Harris²,

Park³

et al. 1970

Enzymol Biol Clin

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The activities of eleven enzymes have been studied quantitatively in the extensor digitorum longus and soleus muscles of rats. Creatine kinase, adenylate kinase, AMP-deaminase, phosphorylase and acid cathepsin were found to have higher specific activities in EDL than SOL. Succinate-INT reductase was found to have the same specific activity in both muscles. Glutamate dehydrogenase, acid a-glucosidase, acid and neutral ribonucléase, and alkaline cathepsin were found to have higher specific activities in SOL than EDL. These findings are discussed with reference to what is known of the physiological roles and subcellular distributions of these enzymes, and with reference to alterations in muscle enzyme activities in muscular dystrophy.

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Section: Determination Of Enzyme Activitiessupporting

confidence: 79%

Quantitative Enzyme Studies in Extensor Digitorum Longus and Soleus Muscles of Rats

Goldspink¹,

Harris²,

Park³

et al. 1970

Enzymol Biol Clin

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“…Roncalés et al (7) reported ultrasonic destabilization of lamb liver lysosomal membranes and activation of proteolysis in extracted lamb longissimus thoracis et lumborum (LTL) muscle fibres sonicated in solution. Nishihara and Doty (6) reported degradation in extracted collagen macromolecules sonicated in solution with high-intensity sound in the acoustic region, and Stagni and de Bernard (8) reported HIU disruption of isolated lysosomes; both findings if observed in whole meat could lead to improved tenderness. Extensive physical disruption of myofibrillar proteins, enhanced myofibrillar proteolysis or connective tissue disruption in whole meat could lead to a role for HIU in guaranteeing tender meat and upgrading of cheaper cuts.…”

Section: Introductionmentioning

confidence: 96%

The Effects of Pre- and Post-rigor High-intensity Ultrasound Treatment on Aspects of Lamb Tenderness

Lyng

Allen

McKenna

1998

LWT - Food Science and Technology

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“…(1) 600 mg muscle from dy/dy and control mice was homogenized with a VirTis homogenizer (model '45') for 2 X 1 min in 3 ml sucrose-histidine-heparin [11], (2) The homogenates were centrifuged at 600 g for 10 min and the superna tant (3) was centrifuged at 8.000 g for 30 min in 13 X 51 mm Beck man tubes (344057) with a Beckman LB-70 ultracentrifuge (Beck man Instruments Inc., Palo Alto, Calif.) supplied with a SW 50.1 rotor. The residue was discarded.…”

Section: Methodsmentioning

confidence: 99%

Changes of Soluble Glycoproteins in Dystrophic <i>(dy/dy)</i> Mouse Muscle Shown by Lectin Binding

et al. 1992

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Lectin binding sites in skeletal muscle from normal and dystrophic (dy/dy) C57 BL/6J mice were demonstrated by use of histochemistry and electrophoresis combined with electron microscopy. The following lectins were used: Canavalia ensiformis Con A, Triticum vulgaris (WGA), Glycine max (SBA), Griffonia simplicifolia (GS II), Arachis hypogaea (PNA), Pisum sativum (PSA) and Lens culinaris (LCA). After incubation of frozen sections with Con A, WGA, GS II, PSA and LCA a sarcoplasmic staining was observed in both normal and dystrophic muscle. The most consistent light microscopic observations in the dystrophic muscles were a decreased staining intensity of the sarcoplasm after incubation with Con A, WGA, PSA and LCA, but not with GS II, and a strong staining of the interfiber connective tissue. Supernatants, deprived of organelles and membranes, were prepared from normal and dystrophic muscle by high speed centrifugation. Lectin stained Western blots of the supernatant from dystrophic muscle showed two bands (120 and 67 K) with high affinities to avidin. Further this supernatant contained two glycoprotein bands (180 and 140 K) with affinities to Con A and a number of glycoprotein bands with apparent molecular weights below 67 K showing affinities to LCA and PSA. None of these glycoprotein bands could be detected in the supernatant from normal muscle. These changes of the muscle carbohydrate components might be involved in the expression of the dystrophic syndrome This seems to be the first report on changes of soluble glycoproteins in muscular dystrophy.

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Lysosomal enzyme activity in rat and beef skeletal muscle

Cited by 58 publications

References 22 publications

Quantitative Enzyme Studies in Extensor Digitorum Longus and Soleus Muscles of Rats

Quantitative Enzyme Studies in Extensor Digitorum Longus and Soleus Muscles of Rats

The Effects of Pre- and Post-rigor High-intensity Ultrasound Treatment on Aspects of Lamb Tenderness

Changes of Soluble Glycoproteins in Dystrophic <i>(dy/dy)</i> Mouse Muscle Shown by Lectin Binding

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